HEADER BLOOD CLOTTING 15-APR-09 3H32
TITLE CRYSTAL STRUCTURE OF D-DIMER FROM HUMAN FIBRIN COMPLEXED WITH GLY-HIS-
TITLE 2 ARG-PRO-TYR-AMIDE
CAVEAT 3H32 INCORRECT STEREOCHEMISTRY AT CARBOHYDRATES: NAG B 471, NAG B
CAVEAT 2 3H32 477, NAG E 471, NAG E 477, MAN B 473, SIA E 479.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIBRINOGEN ALPHA CHAIN;
COMPND 3 CHAIN: A, D;
COMPND 4 FRAGMENT: UNP RESIDUES 20-216;
COMPND 5 SYNONYM: FIBRINOPEPTIDE A;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: FIBRINOGEN BETA CHAIN;
COMPND 8 CHAIN: B, E;
COMPND 9 FRAGMENT: UNP RESIDUES 31-488;
COMPND 10 SYNONYM: FIBRINOPEPTIDE B;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: FIBRINOGEN GAMMA CHAIN, ISOFORM GAMMA-A;
COMPND 13 CHAIN: C, F;
COMPND 14 FRAGMENT: UNP RESIDUES 27-437;
COMPND 15 MOL_ID: 4;
COMPND 16 MOLECULE: FIBRIN B KNOB PENTAPEPTIDE;
COMPND 17 CHAIN: M, N;
COMPND 18 FRAGMENT: UNP RESIDUES 22-26;
COMPND 19 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 TISSUE: BLOOD PLASMA;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 8 ORGANISM_COMMON: HUMAN;
SOURCE 9 ORGANISM_TAXID: 9606;
SOURCE 10 TISSUE: BLOOD PLASMA;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 TISSUE: BLOOD PLASMA;
SOURCE 16 MOL_ID: 4;
SOURCE 17 SYNTHETIC: YES;
SOURCE 18 OTHER_DETAILS: SYNTHETIC PEPTIDE BASED ON THE BOVINE (BOS TAURUS)
SOURCE 19 FIBRINOPEPTIDE B, P02676, FIBB_BOVIN, SEQUENCE POSITION 22-26
KEYWDS FIBRINOGEN, FIBRIN CLOTS, BLOOD CLOTTING, AMYLOID, AMYLOIDOSIS, BLOOD
KEYWDS 2 COAGULATION, DISEASE MUTATION, DISULFIDE BOND, GLYCOPROTEIN,
KEYWDS 3 ISOPEPTIDE BOND, PHOSPHOPROTEIN, SECRETED, PYRROLIDONE CARBOXYLIC
KEYWDS 4 ACID, SULFATION, CDNA FLJ75335, TRANSCRIPT VARIANT GAMMA-A, MRNA,
KEYWDS 5 ISOFORM CRA_M
EXPDTA X-RAY DIFFRACTION
AUTHOR R.F.DOOLITTLE,L.PANDI
REVDAT 4 13-JUL-11 3H32 1 VERSN
REVDAT 3 15-SEP-09 3H32 1 JRNL
REVDAT 2 11-AUG-09 3H32 1 HEADER
REVDAT 1 28-JUL-09 3H32 0
JRNL AUTH L.PANDI,J.M.KOLLMAN,F.LOPEZ-LIRA,J.M.BURROWS,M.RILEY,
JRNL AUTH 2 R.F.DOOLITTLE
JRNL TITL TWO FAMILIES OF SYNTHETIC PEPTIDES THAT ENHANCE FIBRIN
JRNL TITL 2 TURBIDITY AND DELAY FIBRINOLYSIS BY DIFFERENT MECHANISMS.
JRNL REF BIOCHEMISTRY V. 48 7201 2009
JRNL REFN ISSN 0006-2960
JRNL PMID 19588915
JRNL DOI 10.1021/BI900647G
REMARK 2
REMARK 2 RESOLUTION. 3.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 75.5
REMARK 3 NUMBER OF REFLECTIONS : 25002
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.263
REMARK 3 FREE R VALUE : 0.320
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1244
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.73
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11030
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 216
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.013
REMARK 3 BOND ANGLES (DEGREES) : 1.68
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3H32 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-APR-09.
REMARK 100 THE RCSB ID CODE IS RCSB052629.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-OCT-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI(220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31584
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1FZE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: EQUAL VOLUMES OF (A) 5 MG/ML D-DIMER,
REMARK 280 0.5 MM GHRPYAM, 0.3 MM GPRPAM, 0.05 M TRIS-HCL PH 8.0 AND (B) 1%
REMARK 280 PEG 3350, 1 MM IODOACETAMIDE, 1 MM CACL2, 2MM SODIUM AZIDE, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 132.36000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.66000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 132.36000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 48.66000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: D-DIMER IS COMPOSED OF TWO (IDENTICAL) THREE-CHAINED
REMARK 300 MOIETIES CROSS-LINKED NEAR THE CARBOXYL-TERMINI OF THE GAMMA CHAINS.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 22010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 57610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -144.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, M, N
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 1
REMARK 465 ASP A 2
REMARK 465 SER A 3
REMARK 465 GLY A 4
REMARK 465 GLU A 5
REMARK 465 GLY A 6
REMARK 465 ASP A 7
REMARK 465 PHE A 8
REMARK 465 LEU A 9
REMARK 465 ALA A 10
REMARK 465 GLU A 11
REMARK 465 GLY A 12
REMARK 465 GLY A 13
REMARK 465 GLY A 14
REMARK 465 VAL A 15
REMARK 465 ARG A 16
REMARK 465 GLY A 17
REMARK 465 PRO A 18
REMARK 465 ARG A 19
REMARK 465 VAL A 20
REMARK 465 VAL A 21
REMARK 465 GLU A 22
REMARK 465 ARG A 23
REMARK 465 HIS A 24
REMARK 465 GLN A 25
REMARK 465 SER A 26
REMARK 465 ALA A 27
REMARK 465 CYS A 28
REMARK 465 LYS A 29
REMARK 465 ASP A 30
REMARK 465 SER A 31
REMARK 465 ASP A 32
REMARK 465 TRP A 33
REMARK 465 PRO A 34
REMARK 465 PHE A 35
REMARK 465 CYS A 36
REMARK 465 SER A 37
REMARK 465 ASP A 38
REMARK 465 GLU A 39
REMARK 465 ASP A 40
REMARK 465 TRP A 41
REMARK 465 ASN A 42
REMARK 465 TYR A 43
REMARK 465 LYS A 44
REMARK 465 CYS A 45
REMARK 465 PRO A 46
REMARK 465 SER A 47
REMARK 465 GLY A 48
REMARK 465 CYS A 49
REMARK 465 ARG A 50
REMARK 465 MET A 51
REMARK 465 LYS A 52
REMARK 465 GLY A 53
REMARK 465 LEU A 54
REMARK 465 ILE A 55
REMARK 465 ASP A 56
REMARK 465 GLU A 57
REMARK 465 VAL A 58
REMARK 465 ASN A 59
REMARK 465 GLN A 60
REMARK 465 ASP A 61
REMARK 465 PHE A 62
REMARK 465 THR A 63
REMARK 465 ASN A 64
REMARK 465 ARG A 65
REMARK 465 ILE A 66
REMARK 465 ASN A 67
REMARK 465 LYS A 68
REMARK 465 LEU A 69
REMARK 465 LYS A 70
REMARK 465 ASN A 71
REMARK 465 SER A 72
REMARK 465 LEU A 73
REMARK 465 PHE A 74
REMARK 465 GLU A 75
REMARK 465 TYR A 76
REMARK 465 GLN A 77
REMARK 465 LYS A 78
REMARK 465 ASN A 79
REMARK 465 ASN A 80
REMARK 465 LYS A 81
REMARK 465 ASP A 82
REMARK 465 SER A 83
REMARK 465 HIS A 84
REMARK 465 SER A 85
REMARK 465 LEU A 86
REMARK 465 THR A 87
REMARK 465 THR A 88
REMARK 465 ASN A 89
REMARK 465 ILE A 90
REMARK 465 MET A 91
REMARK 465 GLU A 92
REMARK 465 ILE A 93
REMARK 465 LEU A 94
REMARK 465 ARG A 95
REMARK 465 GLY A 96
REMARK 465 ASP A 97
REMARK 465 PHE A 98
REMARK 465 SER A 99
REMARK 465 SER A 100
REMARK 465 ALA A 101
REMARK 465 ASN A 102
REMARK 465 ASN A 103
REMARK 465 ARG A 104
REMARK 465 ASP A 105
REMARK 465 ASN A 106
REMARK 465 THR A 107
REMARK 465 TYR A 108
REMARK 465 ASN A 109
REMARK 465 ARG A 110
REMARK 465 VAL A 111
REMARK 465 SER A 112
REMARK 465 GLU A 113
REMARK 465 ASP A 114
REMARK 465 LEU A 115
REMARK 465 ARG A 116
REMARK 465 SER A 117
REMARK 465 ARG A 118
REMARK 465 LEU A 193
REMARK 465 LEU A 194
REMARK 465 PRO A 195
REMARK 465 SER A 196
REMARK 465 ARG A 197
REMARK 465 GLN B 1
REMARK 465 GLY B 2
REMARK 465 VAL B 3
REMARK 465 ASN B 4
REMARK 465 ASP B 5
REMARK 465 ASN B 6
REMARK 465 GLU B 7
REMARK 465 GLU B 8
REMARK 465 GLY B 9
REMARK 465 PHE B 10
REMARK 465 PHE B 11
REMARK 465 SER B 12
REMARK 465 ALA B 13
REMARK 465 ARG B 14
REMARK 465 GLY B 15
REMARK 465 HIS B 16
REMARK 465 ARG B 17
REMARK 465 PRO B 18
REMARK 465 LEU B 19
REMARK 465 ASP B 20
REMARK 465 LYS B 21
REMARK 465 LYS B 22
REMARK 465 ARG B 23
REMARK 465 GLU B 24
REMARK 465 GLU B 25
REMARK 465 ALA B 26
REMARK 465 PRO B 27
REMARK 465 SER B 28
REMARK 465 LEU B 29
REMARK 465 ARG B 30
REMARK 465 PRO B 31
REMARK 465 ALA B 32
REMARK 465 PRO B 33
REMARK 465 PRO B 34
REMARK 465 PRO B 35
REMARK 465 ILE B 36
REMARK 465 SER B 37
REMARK 465 GLY B 38
REMARK 465 GLY B 39
REMARK 465 GLY B 40
REMARK 465 TYR B 41
REMARK 465 ARG B 42
REMARK 465 ALA B 43
REMARK 465 ARG B 44
REMARK 465 PRO B 45
REMARK 465 ALA B 46
REMARK 465 LYS B 47
REMARK 465 ALA B 48
REMARK 465 ALA B 49
REMARK 465 ALA B 50
REMARK 465 THR B 51
REMARK 465 GLN B 52
REMARK 465 LYS B 53
REMARK 465 LYS B 54
REMARK 465 VAL B 55
REMARK 465 GLU B 56
REMARK 465 ARG B 57
REMARK 465 LYS B 58
REMARK 465 ALA B 59
REMARK 465 PRO B 60
REMARK 465 ASP B 61
REMARK 465 ALA B 62
REMARK 465 GLY B 63
REMARK 465 GLY B 64
REMARK 465 CYS B 65
REMARK 465 LEU B 66
REMARK 465 HIS B 67
REMARK 465 ALA B 68
REMARK 465 ASP B 69
REMARK 465 PRO B 70
REMARK 465 ASP B 71
REMARK 465 LEU B 72
REMARK 465 GLY B 73
REMARK 465 VAL B 74
REMARK 465 LEU B 75
REMARK 465 CYS B 76
REMARK 465 PRO B 77
REMARK 465 THR B 78
REMARK 465 GLY B 79
REMARK 465 CYS B 80
REMARK 465 GLN B 81
REMARK 465 LEU B 82
REMARK 465 GLN B 83
REMARK 465 GLU B 84
REMARK 465 ALA B 85
REMARK 465 LEU B 86
REMARK 465 LEU B 87
REMARK 465 GLN B 88
REMARK 465 GLN B 89
REMARK 465 GLU B 90
REMARK 465 ARG B 91
REMARK 465 PRO B 92
REMARK 465 ILE B 93
REMARK 465 ARG B 94
REMARK 465 ASN B 95
REMARK 465 SER B 96
REMARK 465 VAL B 97
REMARK 465 ASP B 98
REMARK 465 GLU B 99
REMARK 465 LEU B 100
REMARK 465 ASN B 101
REMARK 465 ASN B 102
REMARK 465 ASN B 103
REMARK 465 VAL B 104
REMARK 465 GLU B 105
REMARK 465 ALA B 106
REMARK 465 VAL B 107
REMARK 465 SER B 108
REMARK 465 GLN B 109
REMARK 465 THR B 110
REMARK 465 SER B 111
REMARK 465 SER B 112
REMARK 465 SER B 113
REMARK 465 SER B 114
REMARK 465 PHE B 115
REMARK 465 GLN B 116
REMARK 465 TYR B 117
REMARK 465 MET B 118
REMARK 465 TYR B 119
REMARK 465 LEU B 120
REMARK 465 LEU B 121
REMARK 465 LYS B 122
REMARK 465 ASP B 123
REMARK 465 LEU B 124
REMARK 465 TRP B 125
REMARK 465 GLN B 126
REMARK 465 LYS B 127
REMARK 465 ARG B 128
REMARK 465 GLN B 129
REMARK 465 LYS B 130
REMARK 465 GLN B 131
REMARK 465 VAL B 132
REMARK 465 LYS B 133
REMARK 465 ASP B 134
REMARK 465 ASN B 135
REMARK 465 GLU B 136
REMARK 465 ASN B 137
REMARK 465 VAL B 138
REMARK 465 VAL B 139
REMARK 465 ASN B 140
REMARK 465 GLU B 141
REMARK 465 TYR B 142
REMARK 465 SER B 143
REMARK 465 SER B 144
REMARK 465 GLU B 145
REMARK 465 LEU B 146
REMARK 465 GLU B 147
REMARK 465 LYS B 148
REMARK 465 HIS B 149
REMARK 465 GLN B 150
REMARK 465 LYS C 95
REMARK 465 TYR C 96
REMARK 465 GLN C 398
REMARK 465 GLN C 399
REMARK 465 HIS C 400
REMARK 465 HIS C 401
REMARK 465 LEU C 402
REMARK 465 GLY C 403
REMARK 465 GLY C 404
REMARK 465 ALA C 405
REMARK 465 LYS C 406
REMARK 465 GLN C 407
REMARK 465 ALA C 408
REMARK 465 GLY C 409
REMARK 465 ASP C 410
REMARK 465 VAL C 411
REMARK 465 ALA D 1
REMARK 465 ASP D 2
REMARK 465 SER D 3
REMARK 465 GLY D 4
REMARK 465 GLU D 5
REMARK 465 GLY D 6
REMARK 465 ASP D 7
REMARK 465 PHE D 8
REMARK 465 LEU D 9
REMARK 465 ALA D 10
REMARK 465 GLU D 11
REMARK 465 GLY D 12
REMARK 465 GLY D 13
REMARK 465 GLY D 14
REMARK 465 VAL D 15
REMARK 465 ARG D 16
REMARK 465 GLY D 17
REMARK 465 PRO D 18
REMARK 465 ARG D 19
REMARK 465 VAL D 20
REMARK 465 VAL D 21
REMARK 465 GLU D 22
REMARK 465 ARG D 23
REMARK 465 HIS D 24
REMARK 465 GLN D 25
REMARK 465 SER D 26
REMARK 465 ALA D 27
REMARK 465 CYS D 28
REMARK 465 LYS D 29
REMARK 465 ASP D 30
REMARK 465 SER D 31
REMARK 465 ASP D 32
REMARK 465 TRP D 33
REMARK 465 PRO D 34
REMARK 465 PHE D 35
REMARK 465 CYS D 36
REMARK 465 SER D 37
REMARK 465 ASP D 38
REMARK 465 GLU D 39
REMARK 465 ASP D 40
REMARK 465 TRP D 41
REMARK 465 ASN D 42
REMARK 465 TYR D 43
REMARK 465 LYS D 44
REMARK 465 CYS D 45
REMARK 465 PRO D 46
REMARK 465 SER D 47
REMARK 465 GLY D 48
REMARK 465 CYS D 49
REMARK 465 ARG D 50
REMARK 465 MET D 51
REMARK 465 LYS D 52
REMARK 465 GLY D 53
REMARK 465 LEU D 54
REMARK 465 ILE D 55
REMARK 465 ASP D 56
REMARK 465 GLU D 57
REMARK 465 VAL D 58
REMARK 465 ASN D 59
REMARK 465 GLN D 60
REMARK 465 ASP D 61
REMARK 465 PHE D 62
REMARK 465 THR D 63
REMARK 465 ASN D 64
REMARK 465 ARG D 65
REMARK 465 ILE D 66
REMARK 465 ASN D 67
REMARK 465 LYS D 68
REMARK 465 LEU D 69
REMARK 465 LYS D 70
REMARK 465 ASN D 71
REMARK 465 SER D 72
REMARK 465 LEU D 73
REMARK 465 PHE D 74
REMARK 465 GLU D 75
REMARK 465 TYR D 76
REMARK 465 GLN D 77
REMARK 465 LYS D 78
REMARK 465 ASN D 79
REMARK 465 ASN D 80
REMARK 465 LYS D 81
REMARK 465 ASP D 82
REMARK 465 SER D 83
REMARK 465 HIS D 84
REMARK 465 SER D 85
REMARK 465 LEU D 86
REMARK 465 THR D 87
REMARK 465 THR D 88
REMARK 465 ASN D 89
REMARK 465 ILE D 90
REMARK 465 MET D 91
REMARK 465 GLU D 92
REMARK 465 ILE D 93
REMARK 465 LEU D 94
REMARK 465 ARG D 95
REMARK 465 GLY D 96
REMARK 465 ASP D 97
REMARK 465 PHE D 98
REMARK 465 SER D 99
REMARK 465 SER D 100
REMARK 465 ALA D 101
REMARK 465 ASN D 102
REMARK 465 ASN D 103
REMARK 465 ARG D 104
REMARK 465 ASP D 105
REMARK 465 ASN D 106
REMARK 465 THR D 107
REMARK 465 TYR D 108
REMARK 465 ASN D 109
REMARK 465 ARG D 110
REMARK 465 VAL D 111
REMARK 465 SER D 112
REMARK 465 GLU D 113
REMARK 465 ASP D 114
REMARK 465 LEU D 115
REMARK 465 ARG D 116
REMARK 465 SER D 117
REMARK 465 ARG D 118
REMARK 465 LEU D 193
REMARK 465 LEU D 194
REMARK 465 PRO D 195
REMARK 465 SER D 196
REMARK 465 ARG D 197
REMARK 465 GLN E 1
REMARK 465 GLY E 2
REMARK 465 VAL E 3
REMARK 465 ASN E 4
REMARK 465 ASP E 5
REMARK 465 ASN E 6
REMARK 465 GLU E 7
REMARK 465 GLU E 8
REMARK 465 GLY E 9
REMARK 465 PHE E 10
REMARK 465 PHE E 11
REMARK 465 SER E 12
REMARK 465 ALA E 13
REMARK 465 ARG E 14
REMARK 465 GLY E 15
REMARK 465 HIS E 16
REMARK 465 ARG E 17
REMARK 465 PRO E 18
REMARK 465 LEU E 19
REMARK 465 ASP E 20
REMARK 465 LYS E 21
REMARK 465 LYS E 22
REMARK 465 ARG E 23
REMARK 465 GLU E 24
REMARK 465 GLU E 25
REMARK 465 ALA E 26
REMARK 465 PRO E 27
REMARK 465 SER E 28
REMARK 465 LEU E 29
REMARK 465 ARG E 30
REMARK 465 PRO E 31
REMARK 465 ALA E 32
REMARK 465 PRO E 33
REMARK 465 PRO E 34
REMARK 465 PRO E 35
REMARK 465 ILE E 36
REMARK 465 SER E 37
REMARK 465 GLY E 38
REMARK 465 GLY E 39
REMARK 465 GLY E 40
REMARK 465 TYR E 41
REMARK 465 ARG E 42
REMARK 465 ALA E 43
REMARK 465 ARG E 44
REMARK 465 PRO E 45
REMARK 465 ALA E 46
REMARK 465 LYS E 47
REMARK 465 ALA E 48
REMARK 465 ALA E 49
REMARK 465 ALA E 50
REMARK 465 THR E 51
REMARK 465 GLN E 52
REMARK 465 LYS E 53
REMARK 465 LYS E 54
REMARK 465 VAL E 55
REMARK 465 GLU E 56
REMARK 465 ARG E 57
REMARK 465 LYS E 58
REMARK 465 ALA E 59
REMARK 465 PRO E 60
REMARK 465 ASP E 61
REMARK 465 ALA E 62
REMARK 465 GLY E 63
REMARK 465 GLY E 64
REMARK 465 CYS E 65
REMARK 465 LEU E 66
REMARK 465 HIS E 67
REMARK 465 ALA E 68
REMARK 465 ASP E 69
REMARK 465 PRO E 70
REMARK 465 ASP E 71
REMARK 465 LEU E 72
REMARK 465 GLY E 73
REMARK 465 VAL E 74
REMARK 465 LEU E 75
REMARK 465 CYS E 76
REMARK 465 PRO E 77
REMARK 465 THR E 78
REMARK 465 GLY E 79
REMARK 465 CYS E 80
REMARK 465 GLN E 81
REMARK 465 LEU E 82
REMARK 465 GLN E 83
REMARK 465 GLU E 84
REMARK 465 ALA E 85
REMARK 465 LEU E 86
REMARK 465 LEU E 87
REMARK 465 GLN E 88
REMARK 465 GLN E 89
REMARK 465 GLU E 90
REMARK 465 ARG E 91
REMARK 465 PRO E 92
REMARK 465 ILE E 93
REMARK 465 ARG E 94
REMARK 465 ASN E 95
REMARK 465 SER E 96
REMARK 465 VAL E 97
REMARK 465 ASP E 98
REMARK 465 GLU E 99
REMARK 465 LEU E 100
REMARK 465 ASN E 101
REMARK 465 ASN E 102
REMARK 465 ASN E 103
REMARK 465 VAL E 104
REMARK 465 GLU E 105
REMARK 465 ALA E 106
REMARK 465 VAL E 107
REMARK 465 SER E 108
REMARK 465 GLN E 109
REMARK 465 THR E 110
REMARK 465 SER E 111
REMARK 465 SER E 112
REMARK 465 SER E 113
REMARK 465 SER E 114
REMARK 465 PHE E 115
REMARK 465 GLN E 116
REMARK 465 TYR E 117
REMARK 465 MET E 118
REMARK 465 TYR E 119
REMARK 465 LEU E 120
REMARK 465 LEU E 121
REMARK 465 LYS E 122
REMARK 465 ASP E 123
REMARK 465 LEU E 124
REMARK 465 TRP E 125
REMARK 465 GLN E 126
REMARK 465 LYS E 127
REMARK 465 ARG E 128
REMARK 465 GLN E 129
REMARK 465 LYS E 130
REMARK 465 GLN E 131
REMARK 465 VAL E 132
REMARK 465 LYS E 133
REMARK 465 ASP E 134
REMARK 465 ASN E 135
REMARK 465 GLU E 136
REMARK 465 ASN E 137
REMARK 465 VAL E 138
REMARK 465 VAL E 139
REMARK 465 ASN E 140
REMARK 465 GLU E 141
REMARK 465 TYR E 142
REMARK 465 SER E 143
REMARK 465 SER E 144
REMARK 465 GLU E 145
REMARK 465 LEU E 146
REMARK 465 GLU E 147
REMARK 465 LYS E 148
REMARK 465 HIS E 149
REMARK 465 GLN E 150
REMARK 465 LYS F 95
REMARK 465 TYR F 96
REMARK 465 THR F 393
REMARK 465 ILE F 394
REMARK 465 GLY F 395
REMARK 465 GLU F 396
REMARK 465 GLY F 397
REMARK 465 GLN F 398
REMARK 465 GLN F 399
REMARK 465 HIS F 400
REMARK 465 HIS F 401
REMARK 465 LEU F 402
REMARK 465 GLY F 403
REMARK 465 GLY F 404
REMARK 465 ALA F 405
REMARK 465 LYS F 406
REMARK 465 GLN F 407
REMARK 465 ALA F 408
REMARK 465 GLY F 409
REMARK 465 ASP F 410
REMARK 465 VAL F 411
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS A 165 CA - CB - SG ANGL. DEV. = -17.4 DEGREES
REMARK 500 CYS D 161 CA - CB - SG ANGL. DEV. = 11.8 DEGREES
REMARK 500 PRO E 229 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 164 -45.45 -165.62
REMARK 500 SER A 166 -75.89 -34.08
REMARK 500 VAL A 188 61.77 -111.86
REMARK 500 ILE A 189 -108.86 -96.09
REMARK 500 ALA A 190 101.35 -54.80
REMARK 500 ILE B 153 -7.21 -37.64
REMARK 500 CYS B 193 26.73 -71.07
REMARK 500 PRO B 196 173.06 -50.33
REMARK 500 SER B 222 60.43 -102.26
REMARK 500 PRO B 229 -6.32 -58.59
REMARK 500 ARG B 237 -175.14 -58.74
REMARK 500 VAL B 238 167.18 164.20
REMARK 500 ASN B 243 -44.29 -167.78
REMARK 500 GLU B 245 83.89 43.12
REMARK 500 ASN B 246 -35.71 76.63
REMARK 500 GLN B 256 -18.27 -173.42
REMARK 500 ASP B 257 1.08 -158.46
REMARK 500 LYS B 265 -165.64 -66.98
REMARK 500 THR B 280 68.07 -115.55
REMARK 500 ASP B 281 74.72 43.55
REMARK 500 PRO B 289 -126.35 -62.13
REMARK 500 GLU B 291 123.92 66.22
REMARK 500 TYR B 292 -174.84 -173.89
REMARK 500 ASP B 316 -162.01 -73.95
REMARK 500 ASP B 320 126.83 -32.49
REMARK 500 THR B 330 107.49 -161.77
REMARK 500 ASN B 336 45.70 -108.20
REMARK 500 GLN B 339 175.53 -54.58
REMARK 500 LYS B 344 67.47 61.49
REMARK 500 ALA B 349 -28.31 172.87
REMARK 500 ASN B 351 36.46 -73.56
REMARK 500 MET B 354 -3.73 -145.17
REMARK 500 ALA B 357 173.24 -56.81
REMARK 500 GLU B 363 -35.53 -38.57
REMARK 500 THR B 366 16.75 -59.16
REMARK 500 MET B 373 -177.72 -67.15
REMARK 500 TYR B 378 13.06 -65.09
REMARK 500 ASP B 389 104.54 -56.99
REMARK 500 ASP B 398 77.57 -119.25
REMARK 500 TYR B 404 172.98 -50.94
REMARK 500 ASN B 405 70.59 176.49
REMARK 500 CYS B 407 -40.73 -130.96
REMARK 500 ASN B 411 59.45 -119.10
REMARK 500 ASN B 413 43.74 71.59
REMARK 500 TYR B 416 93.24 -56.98
REMARK 500 ASP B 425 47.40 -75.94
REMARK 500 MET B 426 -35.30 -143.47
REMARK 500 THR B 431 -136.77 -102.92
REMARK 500 VAL B 435 99.14 -63.41
REMARK 500 MET B 438 -44.52 67.12
REMARK 500
REMARK 500 THIS ENTRY HAS 234 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR B 192 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 TYR E 152 24.6 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 381 OD1
REMARK 620 2 ASP B 383 OD1 84.4
REMARK 620 3 TRP B 385 O 165.3 81.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 318 OD1
REMARK 620 2 ASP C 320 OD2 77.1
REMARK 620 3 GLU C 323 O 112.9 169.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 381 OD1
REMARK 620 2 ASP E 383 OD1 102.2
REMARK 620 3 ASP E 383 OD2 74.7 46.8
REMARK 620 4 TRP E 385 O 147.9 80.3 85.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU F 323 O
REMARK 620 2 GLY F 324 N 51.4
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 470
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 471
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 472
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 473
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 474
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL B 478
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA B 479
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 470
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 471
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN E 472
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN E 473
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN E 474
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL E 478
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIA E 479
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2Z4E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF D-DIMER FROM HUMAN FIBRIN COMPLEXED
REMARK 900 WITH GLY-HIS-ARG-PRO-TYR-AMIDE
DBREF 3H32 A 1 197 UNP P02671 FIBA_HUMAN 20 216
DBREF 3H32 B 1 458 UNP P02675 FIBB_HUMAN 31 488
DBREF 3H32 C 95 411 UNP P02679 FIBG_HUMAN 121 437
DBREF 3H32 D 1 197 UNP P02671 FIBA_HUMAN 20 216
DBREF 3H32 E 1 458 UNP P02675 FIBB_HUMAN 31 488
DBREF 3H32 F 95 411 UNP P02679 FIBG_HUMAN 121 437
DBREF 3H32 M 1 5 UNP P02676 FIBB_BOVIN 22 26
DBREF 3H32 N 1 5 UNP P02676 FIBB_BOVIN 22 26
SEQRES 1 A 197 ALA ASP SER GLY GLU GLY ASP PHE LEU ALA GLU GLY GLY
SEQRES 2 A 197 GLY VAL ARG GLY PRO ARG VAL VAL GLU ARG HIS GLN SER
SEQRES 3 A 197 ALA CYS LYS ASP SER ASP TRP PRO PHE CYS SER ASP GLU
SEQRES 4 A 197 ASP TRP ASN TYR LYS CYS PRO SER GLY CYS ARG MET LYS
SEQRES 5 A 197 GLY LEU ILE ASP GLU VAL ASN GLN ASP PHE THR ASN ARG
SEQRES 6 A 197 ILE ASN LYS LEU LYS ASN SER LEU PHE GLU TYR GLN LYS
SEQRES 7 A 197 ASN ASN LYS ASP SER HIS SER LEU THR THR ASN ILE MET
SEQRES 8 A 197 GLU ILE LEU ARG GLY ASP PHE SER SER ALA ASN ASN ARG
SEQRES 9 A 197 ASP ASN THR TYR ASN ARG VAL SER GLU ASP LEU ARG SER
SEQRES 10 A 197 ARG ILE GLU VAL LEU LYS ARG LYS VAL ILE GLU LYS VAL
SEQRES 11 A 197 GLN HIS ILE GLN LEU LEU GLN LYS ASN VAL ARG ALA GLN
SEQRES 12 A 197 LEU VAL ASP MET LYS ARG LEU GLU VAL ASP ILE ASP ILE
SEQRES 13 A 197 LYS ILE ARG SER CYS ARG GLY SER CYS SER ARG ALA LEU
SEQRES 14 A 197 ALA ARG GLU VAL ASP LEU LYS ASP TYR GLU ASP GLN GLN
SEQRES 15 A 197 LYS GLN LEU GLU GLN VAL ILE ALA LYS ASP LEU LEU PRO
SEQRES 16 A 197 SER ARG
SEQRES 1 B 458 GLN GLY VAL ASN ASP ASN GLU GLU GLY PHE PHE SER ALA
SEQRES 2 B 458 ARG GLY HIS ARG PRO LEU ASP LYS LYS ARG GLU GLU ALA
SEQRES 3 B 458 PRO SER LEU ARG PRO ALA PRO PRO PRO ILE SER GLY GLY
SEQRES 4 B 458 GLY TYR ARG ALA ARG PRO ALA LYS ALA ALA ALA THR GLN
SEQRES 5 B 458 LYS LYS VAL GLU ARG LYS ALA PRO ASP ALA GLY GLY CYS
SEQRES 6 B 458 LEU HIS ALA ASP PRO ASP LEU GLY VAL LEU CYS PRO THR
SEQRES 7 B 458 GLY CYS GLN LEU GLN GLU ALA LEU LEU GLN GLN GLU ARG
SEQRES 8 B 458 PRO ILE ARG ASN SER VAL ASP GLU LEU ASN ASN ASN VAL
SEQRES 9 B 458 GLU ALA VAL SER GLN THR SER SER SER SER PHE GLN TYR
SEQRES 10 B 458 MET TYR LEU LEU LYS ASP LEU TRP GLN LYS ARG GLN LYS
SEQRES 11 B 458 GLN VAL LYS ASP ASN GLU ASN VAL VAL ASN GLU TYR SER
SEQRES 12 B 458 SER GLU LEU GLU LYS HIS GLN LEU TYR ILE ASP GLU THR
SEQRES 13 B 458 VAL ASN SER ASN ILE PRO THR ASN LEU ARG VAL LEU ARG
SEQRES 14 B 458 SER ILE LEU GLU ASN LEU ARG SER LYS ILE GLN LYS LEU
SEQRES 15 B 458 GLU SER ASP VAL SER ALA GLN MET GLU TYR CYS ARG THR
SEQRES 16 B 458 PRO CYS THR VAL SER CYS ASN ILE PRO VAL VAL SER GLY
SEQRES 17 B 458 LYS GLU CYS GLU GLU ILE ILE ARG LYS GLY GLY GLU THR
SEQRES 18 B 458 SER GLU MET TYR LEU ILE GLN PRO ASP SER SER VAL LYS
SEQRES 19 B 458 PRO TYR ARG VAL TYR CYS ASP MET ASN THR GLU ASN GLY
SEQRES 20 B 458 GLY TRP THR VAL ILE GLN ASN ARG GLN ASP GLY SER VAL
SEQRES 21 B 458 ASP PHE GLY ARG LYS TRP ASP PRO TYR LYS GLN GLY PHE
SEQRES 22 B 458 GLY ASN VAL ALA THR ASN THR ASP GLY LYS ASN TYR CYS
SEQRES 23 B 458 GLY LEU PRO GLY GLU TYR TRP LEU GLY ASN ASP LYS ILE
SEQRES 24 B 458 SER GLN LEU THR ARG MET GLY PRO THR GLU LEU LEU ILE
SEQRES 25 B 458 GLU MET GLU ASP TRP LYS GLY ASP LYS VAL LYS ALA HIS
SEQRES 26 B 458 TYR GLY GLY PHE THR VAL GLN ASN GLU ALA ASN LYS TYR
SEQRES 27 B 458 GLN ILE SER VAL ASN LYS TYR ARG GLY THR ALA GLY ASN
SEQRES 28 B 458 ALA LEU MET ASP GLY ALA SER GLN LEU MET GLY GLU ASN
SEQRES 29 B 458 ARG THR MET THR ILE HIS ASN GLY MET PHE PHE SER THR
SEQRES 30 B 458 TYR ASP ARG ASP ASN ASP GLY TRP LEU THR SER ASP PRO
SEQRES 31 B 458 ARG LYS GLN CYS SER LYS GLU ASP GLY GLY GLY TRP TRP
SEQRES 32 B 458 TYR ASN ARG CYS HIS ALA ALA ASN PRO ASN GLY ARG TYR
SEQRES 33 B 458 TYR TRP GLY GLY GLN TYR THR TRP ASP MET ALA LYS HIS
SEQRES 34 B 458 GLY THR ASP ASP GLY VAL VAL TRP MET ASN TRP LYS GLY
SEQRES 35 B 458 SER TRP TYR SER MET ARG LYS MET SER MET LYS ILE ARG
SEQRES 36 B 458 PRO PHE PHE
SEQRES 1 C 317 LYS TYR GLU ALA SER ILE LEU THR HIS ASP SER SER ILE
SEQRES 2 C 317 ARG TYR LEU GLN GLU ILE TYR ASN SER ASN ASN GLN LYS
SEQRES 3 C 317 ILE VAL ASN LEU LYS GLU LYS VAL ALA GLN LEU GLU ALA
SEQRES 4 C 317 GLN CYS GLN GLU PRO CYS LYS ASP THR VAL GLN ILE HIS
SEQRES 5 C 317 ASP ILE THR GLY LYS ASP CYS GLN ASP ILE ALA ASN LYS
SEQRES 6 C 317 GLY ALA LYS GLN SER GLY LEU TYR PHE ILE LYS PRO LEU
SEQRES 7 C 317 LYS ALA ASN GLN GLN PHE LEU VAL TYR CYS GLU ILE ASP
SEQRES 8 C 317 GLY SER GLY ASN GLY TRP THR VAL PHE GLN LYS ARG LEU
SEQRES 9 C 317 ASP GLY SER VAL ASP PHE LYS LYS ASN TRP ILE GLN TYR
SEQRES 10 C 317 LYS GLU GLY PHE GLY HIS LEU SER PRO THR GLY THR THR
SEQRES 11 C 317 GLU PHE TRP LEU GLY ASN GLU LYS ILE HIS LEU ILE SER
SEQRES 12 C 317 THR GLN SER ALA ILE PRO TYR ALA LEU ARG VAL GLU LEU
SEQRES 13 C 317 GLU ASP TRP ASN GLY ARG THR SER THR ALA ASP TYR ALA
SEQRES 14 C 317 MET PHE LYS VAL GLY PRO GLU ALA ASP LYS TYR ARG LEU
SEQRES 15 C 317 THR TYR ALA TYR PHE ALA GLY GLY ASP ALA GLY ASP ALA
SEQRES 16 C 317 PHE ASP GLY PHE ASP PHE GLY ASP ASP PRO SER ASP LYS
SEQRES 17 C 317 PHE PHE THR SER HIS ASN GLY MET GLN PHE SER THR TRP
SEQRES 18 C 317 ASP ASN ASP ASN ASP LYS PHE GLU GLY ASN CYS ALA GLU
SEQRES 19 C 317 GLN ASP GLY SER GLY TRP TRP MET ASN LYS CYS HIS ALA
SEQRES 20 C 317 GLY HIS LEU ASN GLY VAL TYR TYR GLN GLY GLY THR TYR
SEQRES 21 C 317 SER LYS ALA SER THR PRO ASN GLY TYR ASP ASN GLY ILE
SEQRES 22 C 317 ILE TRP ALA THR TRP LYS THR ARG TRP TYR SER MET LYS
SEQRES 23 C 317 LYS THR THR MET LYS ILE ILE PRO PHE ASN ARG LEU THR
SEQRES 24 C 317 ILE GLY GLU GLY GLN GLN HIS HIS LEU GLY GLY ALA LYS
SEQRES 25 C 317 GLN ALA GLY ASP VAL
SEQRES 1 D 197 ALA ASP SER GLY GLU GLY ASP PHE LEU ALA GLU GLY GLY
SEQRES 2 D 197 GLY VAL ARG GLY PRO ARG VAL VAL GLU ARG HIS GLN SER
SEQRES 3 D 197 ALA CYS LYS ASP SER ASP TRP PRO PHE CYS SER ASP GLU
SEQRES 4 D 197 ASP TRP ASN TYR LYS CYS PRO SER GLY CYS ARG MET LYS
SEQRES 5 D 197 GLY LEU ILE ASP GLU VAL ASN GLN ASP PHE THR ASN ARG
SEQRES 6 D 197 ILE ASN LYS LEU LYS ASN SER LEU PHE GLU TYR GLN LYS
SEQRES 7 D 197 ASN ASN LYS ASP SER HIS SER LEU THR THR ASN ILE MET
SEQRES 8 D 197 GLU ILE LEU ARG GLY ASP PHE SER SER ALA ASN ASN ARG
SEQRES 9 D 197 ASP ASN THR TYR ASN ARG VAL SER GLU ASP LEU ARG SER
SEQRES 10 D 197 ARG ILE GLU VAL LEU LYS ARG LYS VAL ILE GLU LYS VAL
SEQRES 11 D 197 GLN HIS ILE GLN LEU LEU GLN LYS ASN VAL ARG ALA GLN
SEQRES 12 D 197 LEU VAL ASP MET LYS ARG LEU GLU VAL ASP ILE ASP ILE
SEQRES 13 D 197 LYS ILE ARG SER CYS ARG GLY SER CYS SER ARG ALA LEU
SEQRES 14 D 197 ALA ARG GLU VAL ASP LEU LYS ASP TYR GLU ASP GLN GLN
SEQRES 15 D 197 LYS GLN LEU GLU GLN VAL ILE ALA LYS ASP LEU LEU PRO
SEQRES 16 D 197 SER ARG
SEQRES 1 E 458 GLN GLY VAL ASN ASP ASN GLU GLU GLY PHE PHE SER ALA
SEQRES 2 E 458 ARG GLY HIS ARG PRO LEU ASP LYS LYS ARG GLU GLU ALA
SEQRES 3 E 458 PRO SER LEU ARG PRO ALA PRO PRO PRO ILE SER GLY GLY
SEQRES 4 E 458 GLY TYR ARG ALA ARG PRO ALA LYS ALA ALA ALA THR GLN
SEQRES 5 E 458 LYS LYS VAL GLU ARG LYS ALA PRO ASP ALA GLY GLY CYS
SEQRES 6 E 458 LEU HIS ALA ASP PRO ASP LEU GLY VAL LEU CYS PRO THR
SEQRES 7 E 458 GLY CYS GLN LEU GLN GLU ALA LEU LEU GLN GLN GLU ARG
SEQRES 8 E 458 PRO ILE ARG ASN SER VAL ASP GLU LEU ASN ASN ASN VAL
SEQRES 9 E 458 GLU ALA VAL SER GLN THR SER SER SER SER PHE GLN TYR
SEQRES 10 E 458 MET TYR LEU LEU LYS ASP LEU TRP GLN LYS ARG GLN LYS
SEQRES 11 E 458 GLN VAL LYS ASP ASN GLU ASN VAL VAL ASN GLU TYR SER
SEQRES 12 E 458 SER GLU LEU GLU LYS HIS GLN LEU TYR ILE ASP GLU THR
SEQRES 13 E 458 VAL ASN SER ASN ILE PRO THR ASN LEU ARG VAL LEU ARG
SEQRES 14 E 458 SER ILE LEU GLU ASN LEU ARG SER LYS ILE GLN LYS LEU
SEQRES 15 E 458 GLU SER ASP VAL SER ALA GLN MET GLU TYR CYS ARG THR
SEQRES 16 E 458 PRO CYS THR VAL SER CYS ASN ILE PRO VAL VAL SER GLY
SEQRES 17 E 458 LYS GLU CYS GLU GLU ILE ILE ARG LYS GLY GLY GLU THR
SEQRES 18 E 458 SER GLU MET TYR LEU ILE GLN PRO ASP SER SER VAL LYS
SEQRES 19 E 458 PRO TYR ARG VAL TYR CYS ASP MET ASN THR GLU ASN GLY
SEQRES 20 E 458 GLY TRP THR VAL ILE GLN ASN ARG GLN ASP GLY SER VAL
SEQRES 21 E 458 ASP PHE GLY ARG LYS TRP ASP PRO TYR LYS GLN GLY PHE
SEQRES 22 E 458 GLY ASN VAL ALA THR ASN THR ASP GLY LYS ASN TYR CYS
SEQRES 23 E 458 GLY LEU PRO GLY GLU TYR TRP LEU GLY ASN ASP LYS ILE
SEQRES 24 E 458 SER GLN LEU THR ARG MET GLY PRO THR GLU LEU LEU ILE
SEQRES 25 E 458 GLU MET GLU ASP TRP LYS GLY ASP LYS VAL LYS ALA HIS
SEQRES 26 E 458 TYR GLY GLY PHE THR VAL GLN ASN GLU ALA ASN LYS TYR
SEQRES 27 E 458 GLN ILE SER VAL ASN LYS TYR ARG GLY THR ALA GLY ASN
SEQRES 28 E 458 ALA LEU MET ASP GLY ALA SER GLN LEU MET GLY GLU ASN
SEQRES 29 E 458 ARG THR MET THR ILE HIS ASN GLY MET PHE PHE SER THR
SEQRES 30 E 458 TYR ASP ARG ASP ASN ASP GLY TRP LEU THR SER ASP PRO
SEQRES 31 E 458 ARG LYS GLN CYS SER LYS GLU ASP GLY GLY GLY TRP TRP
SEQRES 32 E 458 TYR ASN ARG CYS HIS ALA ALA ASN PRO ASN GLY ARG TYR
SEQRES 33 E 458 TYR TRP GLY GLY GLN TYR THR TRP ASP MET ALA LYS HIS
SEQRES 34 E 458 GLY THR ASP ASP GLY VAL VAL TRP MET ASN TRP LYS GLY
SEQRES 35 E 458 SER TRP TYR SER MET ARG LYS MET SER MET LYS ILE ARG
SEQRES 36 E 458 PRO PHE PHE
SEQRES 1 F 317 LYS TYR GLU ALA SER ILE LEU THR HIS ASP SER SER ILE
SEQRES 2 F 317 ARG TYR LEU GLN GLU ILE TYR ASN SER ASN ASN GLN LYS
SEQRES 3 F 317 ILE VAL ASN LEU LYS GLU LYS VAL ALA GLN LEU GLU ALA
SEQRES 4 F 317 GLN CYS GLN GLU PRO CYS LYS ASP THR VAL GLN ILE HIS
SEQRES 5 F 317 ASP ILE THR GLY LYS ASP CYS GLN ASP ILE ALA ASN LYS
SEQRES 6 F 317 GLY ALA LYS GLN SER GLY LEU TYR PHE ILE LYS PRO LEU
SEQRES 7 F 317 LYS ALA ASN GLN GLN PHE LEU VAL TYR CYS GLU ILE ASP
SEQRES 8 F 317 GLY SER GLY ASN GLY TRP THR VAL PHE GLN LYS ARG LEU
SEQRES 9 F 317 ASP GLY SER VAL ASP PHE LYS LYS ASN TRP ILE GLN TYR
SEQRES 10 F 317 LYS GLU GLY PHE GLY HIS LEU SER PRO THR GLY THR THR
SEQRES 11 F 317 GLU PHE TRP LEU GLY ASN GLU LYS ILE HIS LEU ILE SER
SEQRES 12 F 317 THR GLN SER ALA ILE PRO TYR ALA LEU ARG VAL GLU LEU
SEQRES 13 F 317 GLU ASP TRP ASN GLY ARG THR SER THR ALA ASP TYR ALA
SEQRES 14 F 317 MET PHE LYS VAL GLY PRO GLU ALA ASP LYS TYR ARG LEU
SEQRES 15 F 317 THR TYR ALA TYR PHE ALA GLY GLY ASP ALA GLY ASP ALA
SEQRES 16 F 317 PHE ASP GLY PHE ASP PHE GLY ASP ASP PRO SER ASP LYS
SEQRES 17 F 317 PHE PHE THR SER HIS ASN GLY MET GLN PHE SER THR TRP
SEQRES 18 F 317 ASP ASN ASP ASN ASP LYS PHE GLU GLY ASN CYS ALA GLU
SEQRES 19 F 317 GLN ASP GLY SER GLY TRP TRP MET ASN LYS CYS HIS ALA
SEQRES 20 F 317 GLY HIS LEU ASN GLY VAL TYR TYR GLN GLY GLY THR TYR
SEQRES 21 F 317 SER LYS ALA SER THR PRO ASN GLY TYR ASP ASN GLY ILE
SEQRES 22 F 317 ILE TRP ALA THR TRP LYS THR ARG TRP TYR SER MET LYS
SEQRES 23 F 317 LYS THR THR MET LYS ILE ILE PRO PHE ASN ARG LEU THR
SEQRES 24 F 317 ILE GLY GLU GLY GLN GLN HIS HIS LEU GLY GLY ALA LYS
SEQRES 25 F 317 GLN ALA GLY ASP VAL
SEQRES 1 M 5 GLY HIS ARG PRO TYR
SEQRES 1 N 5 GLY HIS ARG PRO TYR
MODRES 3H32 ASN B 364 ASN GLYCOSYLATION SITE
MODRES 3H32 ASN E 364 ASN GLYCOSYLATION SITE
HET CA C 501 1
HET CA B 502 1
HET CA F 501 1
HET CA E 502 1
HET NAG B 470 14
HET NAG B 471 14
HET MAN B 472 11
HET MAN B 473 11
HET MAN B 474 11
HET NAG B 477 14
HET GAL B 478 11
HET SIA B 479 20
HET NAG E 470 14
HET NAG E 471 14
HET MAN E 472 11
HET MAN E 473 11
HET MAN E 474 11
HET NAG E 477 14
HET GAL E 478 11
HET SIA E 479 20
HETNAM CA CALCIUM ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM GAL BETA-D-GALACTOSE
HETNAM SIA O-SIALIC ACID
FORMUL 9 CA 4(CA 2+)
FORMUL 13 NAG 6(C8 H15 N O6)
FORMUL 13 MAN 6(C6 H12 O6)
FORMUL 13 GAL 2(C6 H12 O6)
FORMUL 13 SIA 2(C11 H19 N O9)
HELIX 1 1 ARG A 124 LYS A 129 1 6
HELIX 2 2 VAL A 130 CYS A 161 1 32
HELIX 3 3 ARG A 162 SER A 164 5 3
HELIX 4 4 ASP A 174 VAL A 188 1 15
HELIX 5 5 TYR B 152 ASP B 154 5 3
HELIX 6 6 GLU B 155 ASN B 160 1 6
HELIX 7 7 ASN B 160 CYS B 193 1 34
HELIX 8 8 GLU B 210 ARG B 216 1 7
HELIX 9 9 TRP B 266 GLY B 272 1 7
HELIX 10 10 GLY B 295 ARG B 304 1 10
HELIX 11 11 ASN B 333 LYS B 337 5 5
HELIX 12 12 ASN B 351 GLY B 356 1 6
HELIX 13 13 MET B 361 ARG B 365 5 5
HELIX 14 14 GLN B 393 ASP B 398 1 6
HELIX 15 15 ALA C 98 SER C 105 5 8
HELIX 16 16 SER C 106 CYS C 135 1 30
HELIX 17 17 ASP C 152 ALA C 157 1 6
HELIX 18 18 ASN C 207 GLY C 214 1 8
HELIX 19 19 GLY C 229 GLN C 239 1 11
HELIX 20 20 PRO C 269 LYS C 273 5 5
HELIX 21 21 ASP C 288 GLY C 292 5 5
HELIX 22 22 ASN C 325 ASP C 330 1 6
HELIX 23 23 ARG D 124 LYS D 129 1 6
HELIX 24 24 VAL D 130 CYS D 161 1 32
HELIX 25 25 ARG D 162 SER D 164 5 3
HELIX 26 26 ASP D 174 VAL D 188 1 15
HELIX 27 27 TYR E 152 ASP E 154 5 3
HELIX 28 28 GLU E 155 CYS E 193 1 39
HELIX 29 29 GLU E 210 ARG E 216 1 7
HELIX 30 30 LYS E 265 GLN E 271 1 7
HELIX 31 31 GLY E 295 ARG E 304 1 10
HELIX 32 32 ASN E 333 LYS E 337 5 5
HELIX 33 33 MET E 361 ARG E 365 5 5
HELIX 34 34 GLN E 393 ASP E 398 1 6
HELIX 35 35 THR E 423 ALA E 427 5 5
HELIX 36 36 GLU F 97 LEU F 101 5 5
HELIX 37 37 THR F 102 SER F 105 5 4
HELIX 38 38 SER F 106 CYS F 135 1 30
HELIX 39 39 ASP F 152 ALA F 157 1 6
HELIX 40 40 ASN F 207 GLU F 213 1 7
HELIX 41 41 GLY F 229 GLN F 239 1 11
HELIX 42 42 PRO F 269 LYS F 273 5 5
HELIX 43 43 ASP F 288 GLY F 292 5 5
HELIX 44 44 SER F 300 PHE F 304 5 5
HELIX 45 45 ASN F 325 ASP F 330 1 6
HELIX 46 46 SER F 355 THR F 359 5 5
HELIX 47 47 ASN F 390 LEU F 392 5 3
SHEET 1 A 2 THR B 198 VAL B 199 0
SHEET 2 A 2 LYS C 140 ASP C 141 1 O LYS C 140 N VAL B 199
SHEET 1 B 5 MET B 224 ILE B 227 0
SHEET 2 B 5 TYR B 236 ASP B 241 -1 O VAL B 238 N TYR B 225
SHEET 3 B 5 TRP B 249 ASN B 254 -1 O TRP B 249 N ASP B 241
SHEET 4 B 5 TYR B 292 TRP B 293 -1 O TYR B 292 N ASN B 254
SHEET 5 B 5 PHE B 273 GLY B 274 -1 N PHE B 273 O TRP B 293
SHEET 1 C 7 MET B 224 ILE B 227 0
SHEET 2 C 7 TYR B 236 ASP B 241 -1 O VAL B 238 N TYR B 225
SHEET 3 C 7 TRP B 249 ASN B 254 -1 O TRP B 249 N ASP B 241
SHEET 4 C 7 LYS B 449 PRO B 456 -1 O ILE B 454 N THR B 250
SHEET 5 C 7 THR B 308 GLU B 315 -1 N GLU B 309 O ARG B 455
SHEET 6 C 7 LYS B 321 TYR B 326 -1 O TYR B 326 N LEU B 310
SHEET 7 C 7 GLY B 347 THR B 348 -1 O THR B 348 N LYS B 323
SHEET 1 D 2 THR B 278 THR B 280 0
SHEET 2 D 2 LYS B 283 LEU B 288 -1 O LEU B 288 N THR B 278
SHEET 1 E 3 LEU C 166 ILE C 169 0
SHEET 2 E 3 PHE C 178 GLU C 183 -1 O VAL C 180 N TYR C 167
SHEET 3 E 3 TRP C 191 THR C 192 -1 O TRP C 191 N GLU C 183
SHEET 1 F 6 PHE C 215 GLY C 216 0
SHEET 2 F 6 PHE C 226 TRP C 227 -1 O TRP C 227 N PHE C 215
SHEET 3 F 6 GLN C 195 ARG C 197 -1 N LYS C 196 O PHE C 226
SHEET 4 F 6 LYS C 381 MET C 384 -1 O MET C 384 N GLN C 195
SHEET 5 F 6 TYR C 244 GLU C 251 -1 O GLU C 249 N THR C 383
SHEET 6 F 6 ASP C 261 PHE C 265 -1 O TYR C 262 N LEU C 246
SHEET 1 G 3 THR C 257 SER C 258 0
SHEET 2 G 3 TYR C 244 GLU C 251 -1 N LEU C 250 O SER C 258
SHEET 3 G 3 ILE C 387 PRO C 388 -1 O ILE C 387 N ALA C 245
SHEET 1 H 2 SER C 313 THR C 314 0
SHEET 2 H 2 GLY C 333 TRP C 334 -1 O TRP C 334 N SER C 313
SHEET 1 I 2 THR E 198 VAL E 199 0
SHEET 2 I 2 LYS F 140 ASP F 141 1 O LYS F 140 N VAL E 199
SHEET 1 J 6 MET E 224 ILE E 227 0
SHEET 2 J 6 TYR E 236 ASP E 241 -1 O TYR E 236 N ILE E 227
SHEET 3 J 6 TRP E 249 ARG E 255 -1 O TRP E 249 N ASP E 241
SHEET 4 J 6 LYS E 449 PRO E 456 -1 O ILE E 454 N THR E 250
SHEET 5 J 6 MET E 314 GLU E 315 -1 N GLU E 315 O LYS E 449
SHEET 6 J 6 LYS E 321 VAL E 322 -1 O VAL E 322 N MET E 314
SHEET 1 K 6 GLY E 272 GLY E 274 0
SHEET 2 K 6 TYR E 292 LEU E 294 -1 O TRP E 293 N PHE E 273
SHEET 3 K 6 TRP E 249 ARG E 255 -1 N ILE E 252 O LEU E 294
SHEET 4 K 6 LYS E 449 PRO E 456 -1 O ILE E 454 N THR E 250
SHEET 5 K 6 THR E 308 LEU E 311 -1 N GLU E 309 O ARG E 455
SHEET 6 K 6 HIS E 325 TYR E 326 -1 O TYR E 326 N LEU E 310
SHEET 1 L 2 THR E 278 THR E 280 0
SHEET 2 L 2 LYS E 283 LEU E 288 -1 O LEU E 288 N THR E 278
SHEET 1 M 4 ILE F 145 GLY F 150 0
SHEET 2 M 4 LEU F 166 ILE F 169 1 O LEU F 166 N HIS F 146
SHEET 3 M 4 PHE F 178 ILE F 184 -1 O PHE F 178 N ILE F 169
SHEET 4 M 4 GLY F 190 THR F 192 -1 O TRP F 191 N GLU F 183
SHEET 1 N 6 PHE F 215 GLY F 216 0
SHEET 2 N 6 PHE F 226 TRP F 227 -1 O TRP F 227 N PHE F 215
SHEET 3 N 6 GLN F 195 ARG F 197 -1 N LYS F 196 O PHE F 226
SHEET 4 N 6 LYS F 381 PRO F 388 -1 O THR F 382 N ARG F 197
SHEET 5 N 6 TYR F 244 GLU F 251 -1 N GLU F 249 O THR F 383
SHEET 6 N 6 THR F 257 SER F 258 -1 O SER F 258 N LEU F 250
SHEET 1 O 7 PHE F 215 GLY F 216 0
SHEET 2 O 7 PHE F 226 TRP F 227 -1 O TRP F 227 N PHE F 215
SHEET 3 O 7 GLN F 195 ARG F 197 -1 N LYS F 196 O PHE F 226
SHEET 4 O 7 LYS F 381 PRO F 388 -1 O THR F 382 N ARG F 197
SHEET 5 O 7 TYR F 244 GLU F 251 -1 N GLU F 249 O THR F 383
SHEET 6 O 7 ASP F 261 ALA F 263 -1 O TYR F 262 N LEU F 246
SHEET 7 O 7 TYR F 280 PHE F 281 -1 O TYR F 280 N ALA F 263
SSBOND 1 CYS A 161 CYS C 135 1555 1555 1.92
SSBOND 2 CYS A 161 CYS B 193 1555 1555 2.05
SSBOND 3 CYS A 161 CYS A 165 1555 1555 2.16
SSBOND 4 CYS A 165 CYS B 193 1555 1555 2.01
SSBOND 5 CYS A 165 CYS C 135 1555 1555 2.02
SSBOND 6 CYS B 193 CYS C 135 1555 1555 2.16
SSBOND 7 CYS B 197 CYS C 139 1555 1555 2.05
SSBOND 8 CYS B 201 CYS B 286 1555 1555 2.05
SSBOND 9 CYS B 211 CYS B 240 1555 1555 2.01
SSBOND 10 CYS B 394 CYS B 407 1555 1555 2.04
SSBOND 11 CYS C 153 CYS C 182 1555 1555 2.02
SSBOND 12 CYS C 326 CYS C 339 1555 1555 2.03
SSBOND 13 CYS D 161 CYS D 165 1555 1555 2.06
SSBOND 14 CYS D 161 CYS F 135 1555 1555 2.06
SSBOND 15 CYS D 165 CYS F 135 1555 1555 2.01
SSBOND 16 CYS D 165 CYS E 193 1555 1555 2.04
SSBOND 17 CYS E 193 CYS F 135 1555 1555 2.07
SSBOND 18 CYS E 197 CYS F 139 1555 1555 2.04
SSBOND 19 CYS E 201 CYS E 286 1555 1555 2.04
SSBOND 20 CYS E 211 CYS E 240 1555 1555 2.03
SSBOND 21 CYS E 394 CYS E 407 1555 1555 2.03
SSBOND 22 CYS F 153 CYS F 182 1555 1555 2.03
SSBOND 23 CYS F 326 CYS F 339 1555 1555 2.04
LINK ND2 ASN B 364 C1 NAG B 470 1555 1555 1.45
LINK OD1 ASP B 381 CA CA B 502 1555 1555 2.44
LINK OD1 ASP B 383 CA CA B 502 1555 1555 2.20
LINK O TRP B 385 CA CA B 502 1555 1555 2.05
LINK OD1 ASP C 318 CA CA C 501 1555 1555 2.69
LINK OD2 ASP C 320 CA CA C 501 1555 1555 2.55
LINK O GLU C 323 CA CA C 501 1555 1555 2.21
LINK ND2 ASN E 364 C1 NAG E 470 1555 1555 1.46
LINK OD1 ASP E 381 CA CA E 502 1555 1555 2.24
LINK OD1 ASP E 383 CA CA E 502 1555 1555 2.10
LINK OD2 ASP E 383 CA CA E 502 1555 1555 3.00
LINK O TRP E 385 CA CA E 502 1555 1555 2.31
LINK O GLU F 323 CA CA F 501 1555 1555 2.78
LINK N GLY F 324 CA CA F 501 1555 1555 2.36
LINK O4 NAG B 470 C1 NAG B 471 1555 1555 1.39
LINK O4 NAG B 471 C1 MAN B 472 1555 1555 1.41
LINK O3 MAN B 472 C1 MAN B 474 1555 1555 1.42
LINK O6 MAN B 472 C1 MAN B 473 1555 1555 1.41
LINK O2 MAN B 474 C1 NAG B 477 1555 1555 1.41
LINK O4 NAG B 477 C1 GAL B 478 1555 1555 1.39
LINK O6 GAL B 478 C2 SIA B 479 1555 1555 1.40
LINK O4 NAG E 470 C1 NAG E 471 1555 1555 1.39
LINK O4 NAG E 471 C1 MAN E 472 1555 1555 1.40
LINK O3 MAN E 472 C1 MAN E 474 1555 1555 1.42
LINK O6 MAN E 472 C1 MAN E 473 1555 1555 1.41
LINK O2 MAN E 474 C1 NAG E 477 1555 1555 1.40
LINK O4 NAG E 477 C1 GAL E 478 1555 1555 1.41
LINK O6 GAL E 478 C2 SIA E 479 1555 1555 1.42
CISPEP 1 ARG B 406 CYS B 407 0 -0.96
CISPEP 2 LYS C 338 CYS C 339 0 2.21
CISPEP 3 ARG E 406 CYS E 407 0 -0.83
CISPEP 4 LYS F 338 CYS F 339 0 1.21
SITE 1 AC1 6 ASP C 318 ASP C 320 PHE C 322 GLU C 323
SITE 2 AC1 6 GLY C 324 ASN C 325
SITE 1 AC2 3 ASP B 381 ASP B 383 TRP B 385
SITE 1 AC3 3 GLU F 323 GLY F 324 ASN F 325
SITE 1 AC4 3 ASP E 381 ASP E 383 TRP E 385
SITE 1 AC5 5 MET B 361 ASN B 364 NAG B 471 HIS M 2
SITE 2 AC5 5 PRO M 4
SITE 1 AC6 4 NAG B 470 MAN B 472 MAN B 473 MAN B 474
SITE 1 AC7 4 NAG B 471 MAN B 473 MAN B 474 NAG B 477
SITE 1 AC8 2 NAG B 471 MAN B 472
SITE 1 AC9 3 NAG B 471 MAN B 472 NAG B 477
SITE 1 BC1 4 MAN B 472 MAN B 474 GAL B 478 SIA B 479
SITE 1 BC2 2 NAG B 477 SIA B 479
SITE 1 BC3 3 TRP B 424 NAG B 477 GAL B 478
SITE 1 BC4 5 MET E 361 ASN E 364 NAG E 471 HIS N 2
SITE 2 BC4 5 PRO N 4
SITE 1 BC5 3 NAG E 470 MAN E 472 MAN E 474
SITE 1 BC6 4 NAG E 471 MAN E 473 MAN E 474 NAG E 477
SITE 1 BC7 1 MAN E 472
SITE 1 BC8 3 NAG E 471 MAN E 472 NAG E 477
SITE 1 BC9 3 MAN E 472 MAN E 474 GAL E 478
SITE 1 CC1 2 NAG E 477 SIA E 479
SITE 1 CC2 2 TRP E 424 GAL E 478
CRYST1 264.720 97.320 132.490 90.00 122.78 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.003778 0.000000 0.002433 0.00000
SCALE2 0.000000 0.010275 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008977 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
